4owf

X-ray diffraction
2Å resolution

Crystal structure of the NEMO CoZi in complex with HOIP NZF1 domain

Released:

Function and Biology Details

Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-131553 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NF-kappa-B essential modulator Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 10.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O88522 (Residues: 250-339; Coverage: 22%)
Gene names: Ikbkg, Nemo
Sequence domains: Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator
Structure domains: Nemo cc2-lz domain - 1d5 darpin complex
E3 ubiquitin-protein ligase RNF31 Chain: G
Molecule details ›
Chain: G
Length: 30 amino acids
Theoretical weight: 3.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96EP0 (Residues: 350-379; Coverage: 3%)
Gene names: RNF31, ZIBRA

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P65
Unit cell:
a: 81.41Å b: 81.41Å c: 74.501Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.262 0.259 0.313
Expression system: Escherichia coli BL21